Human BCAM APC‑conjugated Antibody

Basal-Cell Adhesion Molecule (BCAM) and Lutheran blood group glycoprotein (LU) are two alternatively spliced variants of a single immunoglobulin superfamily (IgSF) protein that differ in the length of their cytoplasmic tails. BCAM cDNA encodes a 628 amino acid (aa) residues precursor protein with a putative 31 aa signal peptide, a 597 aa extracellular domain containing three C2 type and two V-type Ig-like domains, a 21 aa transmembrane domain, and a 19 aa cytoplasmic domain. Compared to the 40 aa cytoplasmic domain present in LU, the BCAM cytoplasmic tail lacks the putative Src homology 3 (SH3) binding site that may be involved in mediating intracellular signaling. BCAM/LU has wide tissue distribution and is expressed on erythrocytes, the endothelium of blood vessels and on the basal layer of cells in the epithelia. The expression of BCAM/LU in normal tissues is higher in fetal versus adult tissues. BCAM/LU expression is also upregulated in sickle cell disease red blood cells, in activated keratinocytes and following malignant transformation in some cell types in vivo and in vitro. BCAM/LU has been shown to be an adhesion molecule that binds laminin, a basement membrane protein involved in cell differentiation, adhesion, migration and proliferation.